Evidence map›Paper›PMID 27831485›Full record

ArticleThe Journal of cell biology2016

Analysis of membrane proteins localizing to the inner nuclear envelope in living cells.

Christine J Smoyer, Santharam S Katta, Jennifer M Gardner, Lynn Stoltz, Scott McCroskey, William D Bradford, Melainia McClain, Sarah E Smith, Brian D Slaughter, Jay R Unruh and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed, 96 citations in OpenAlex.

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  13. Mechanisms for assembly of the nucleoplasmic reticulum.Cellular and molecular life sciences : CMLS · 2024
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Christine J SmoyerStowers Institute for Medical Research, Kansas City, MO 64110.ORCID http://orcid.org/0000-0002-6932-8560
Santharam S KattaStowers Institute for Medical Research, Kansas City, MO 64110.ORCID http://orcid.org/0000-0003-2579-8904
Jennifer M GardnerStowers Institute for Medical Research, Kansas City, MO 64110.
Lynn StoltzStowers Institute for Medical Research, Kansas City, MO 64110.
Scott McCroskeyStowers Institute for Medical Research, Kansas City, MO 64110.
William D BradfordStowers Institute for Medical Research, Kansas City, MO 64110.ORCID http://orcid.org/0000-0001-8302-8305
Melainia McClainStowers Institute for Medical Research, Kansas City, MO 64110.ORCID http://orcid.org/0000-0002-8947-9841
Sarah E SmithStowers Institute for Medical Research, Kansas City, MO 64110.
Brian D SlaughterStowers Institute for Medical Research, Kansas City, MO 64110.
Jay R UnruhStowers Institute for Medical Research, Kansas City, MO 64110.
Sue L JaspersenStowers Institute for Medical Research, Kansas City, MO 64110 slj@stowers.org.ORCID http://orcid.org/0000-0001-8312-7063
Stowers Institute for Medical Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding the protein composition of the inner nuclear membrane (INM) is fundamental to elucidating its role in normal nuclear function and in disease; however, few tools exist to examine the INM in living cells, and the INM-specific proteome remains poorly characterized. Here, we adapted split green fluorescent protein (split-GFP) to systematically localize known and predicted integral membrane proteins in Saccharomyces cerevisiae to the INM as opposed to the outer nuclear membrane. Our data suggest that components of the endoplasmic reticulum (ER) as well as other organelles are able to access the INM, particularly if they contain a small extraluminal domain. By pairing split-GFP with fluorescence correlation spectroscopy, we compared the composition of complexes at the INM and ER, finding that at least one is unique: Sbh2, but not Sbh1, has access to the INM. Collectively, our work provides a comprehensive analysis of transmembrane protein localization to the INM and paves the way for further research into INM composition and function.

Indexed as

Endoplasmic ReticulumGenome, FungalGreen Fluorescent ProteinsMembrane ProteinsNuclear EnvelopeProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, FluorescenceGreen Fluorescent ProteinsMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID27831485
PMCPMC5119940
OpenAlexW2555587028

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.